3BP1_HUMAN
ID 3BP1_HUMAN Reviewed; 701 AA.
AC Q9Y3L3; Q5R3N0; Q6IBZ2; Q6ZVL9; Q96HQ5; Q9NSQ9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=SH3 domain-binding protein 1 {ECO:0000312|HGNC:HGNC:10824};
GN Name=SH3BP1 {ECO:0000312|HGNC:HGNC:10824};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-701 (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 360-701 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, INTERACTION WITH EXOC4 AND EXOC8, SUBCELLULAR LOCATION, DOMAIN,
RP AND MUTAGENESIS OF ARG-312.
RX PubMed=21658605; DOI=10.1016/j.molcel.2011.03.032;
RA Parrini M.C., Sadou-Dubourgnoux A., Aoki K., Kunida K., Biondini M.,
RA Hatzoglou A., Poullet P., Formstecher E., Yeaman C., Matsuda M., Rosse C.,
RA Camonis J.;
RT "SH3BP1, an exocyst-associated RhoGAP, inactivates Rac1 at the front to
RT drive cell motility.";
RL Mol. Cell 42:650-661(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP FUNCTION, INTERACTION WITH AFDN; CAPZA1; CD2AP AND CGNL1, SUBCELLULAR
RP LOCATION, AND REGION.
RX PubMed=22891260; DOI=10.1083/jcb.201202094;
RA Elbediwy A., Zihni C., Terry S.J., Clark P., Matter K., Balda M.S.;
RT "Epithelial junction formation requires confinement of Cdc42 activity by a
RT novel SH3BP1 complex.";
RL J. Cell Biol. 198:677-693(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-262; SER-544;
RP SER-550 AND THR-626, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP ALTERNATIVE SPLICING (ISOFORMS LONG BGIN AND SHORT BGIN).
RX PubMed=23223568; DOI=10.1091/mbc.e12-07-0565;
RA Huang T.Y., Michael S., Xu T., Sarkeshik A., Moresco J.J., Yates J.R. III,
RA Masliah E., Bokoch G.M., DerMardirossian C.;
RT "A novel Rac1 GAP splice variant relays poly-Ub accumulation signals to
RT mediate Rac1 inactivation.";
RL Mol. Biol. Cell 24:194-209(2013).
RN [14]
RP FUNCTION, INTERACTION WITH PLXND1, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=24841563; DOI=10.1083/jcb.201309004;
RA Tata A., Stoppel D.C., Hong S., Ben-Zvi A., Xie T., Gu C.;
RT "An image-based RNAi screen identifies SH3BP1 as a key effector of
RT Semaphorin 3E-PlexinD1 signaling.";
RL J. Cell Biol. 205:573-590(2014).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262; SER-264 AND SER-544, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26465210; DOI=10.1038/ncomms9623;
RA Schlam D., Bagshaw R.D., Freeman S.A., Collins R.F., Pawson T., Fairn G.D.,
RA Grinstein S.;
RT "Phosphoinositide 3-kinase enables phagocytosis of large particles by
RT terminating actin assembly through Rac/Cdc42 GTPase-activating proteins.";
RL Nat. Commun. 6:8623-8623(2015).
CC -!- FUNCTION: GTPase activating protein (GAP) which specifically converts
CC GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive
CC GDP-bound form. By specifically inactivating RAC1 at the leading edge
CC of migrating cells, it regulates the spatiotemporal organization of
CC cell protrusions which is important for proper cell migration
CC (PubMed:21658605). Also negatively regulates CDC42 in the process of
CC actin remodeling and the formation of epithelial cell junctions
CC (PubMed:22891260). Through its GAP activity toward RAC1 and/or CDC42
CC plays a specific role in phagocytosis of large particles. Specifically
CC recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large
CC particles engagement, inactivates RAC1 and/or CDC42 allowing the
CC reorganization of the underlying actin cytoskeleton required for
CC engulfment (PubMed:26465210). It also plays a role in angiogenesis and
CC the process of repulsive guidance as part of a semaphorin-plexin
CC signaling pathway. Following the binding of PLXND1 to extracellular
CC SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the
CC intracellular reorganization of the actin cytoskeleton and the collapse
CC of cells (PubMed:24841563). {ECO:0000269|PubMed:21658605,
CC ECO:0000269|PubMed:22891260, ECO:0000269|PubMed:24841563,
CC ECO:0000269|PubMed:26465210}.
CC -!- SUBUNIT: Interacts with RAC1 (By similarity). Interacts with the
CC exocyst via EXOC4 and EXOC8; required for the localization of both
CC SH3BP1 and the exocyst to the leading edge of migrating cells
CC (PubMed:21658605). Interacts with CD2AP and CGNL1; probably part of a
CC complex at cell junctions (PubMed:22891260). Interacts with CAPZA1;
CC recruits CAPZA1 to forming cell junctions (PubMed:22891260). May
CC interact with AFDN (PubMed:22891260). Interacts with PLXND1; they
CC dissociate upon SEMA3E binding to PLXND1 allowing SH3BP1 to transduce
CC downstream signal through RAC1 inactivation (PubMed:24841563).
CC Interacts with ABL1, GRB2 and SRC (via SH3 domain) (By similarity).
CC {ECO:0000250|UniProtKB:P55194, ECO:0000269|PubMed:21658605,
CC ECO:0000269|PubMed:22891260, ECO:0000269|PubMed:24841563}.
CC -!- INTERACTION:
CC Q9Y3L3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-346869, EBI-11096309;
CC Q9Y3L3; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-346869, EBI-742038;
CC Q9Y3L3; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-346869, EBI-10749669;
CC Q9Y3L3; P02671-2: FGA; NbExp=3; IntAct=EBI-346869, EBI-9640259;
CC Q9Y3L3; P54274: TERF1; NbExp=2; IntAct=EBI-346869, EBI-710997;
CC Q9Y3L3; Q15642: TRIP10; NbExp=3; IntAct=EBI-346869, EBI-739936;
CC Q9Y3L3; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-346869, EBI-6550597;
CC -!- SUBCELLULAR LOCATION: Cell projection {ECO:0000269|PubMed:21658605,
CC ECO:0000269|PubMed:24841563}. Cell junction, tight junction
CC {ECO:0000269|PubMed:22891260}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:22891260}. Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:26465210}. Nucleus {ECO:0000269|PubMed:22891260}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:22891260}. Note=Localizes at the
CC leading edge of migrating cells (PubMed:21658605, PubMed:24841563).
CC Accumulation at forming phagocytic cups is PI3 kinase/PI3K-dependent
CC and is specific for sites of large particles engagement and their
CC phosphatidylinositol 3,4,5-triphosphate membrane content
CC (PubMed:26465210). {ECO:0000269|PubMed:21658605,
CC ECO:0000269|PubMed:24841563, ECO:0000269|PubMed:26465210}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y3L3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3L3-2; Sequence=VSP_011373, VSP_011374;
CC Name=Long BGIN {ECO:0000303|PubMed:23223568};
CC IsoId=Q6ZT62-1; Sequence=External;
CC Name=Short BGIN {ECO:0000303|PubMed:23223568};
CC IsoId=Q6ZT62-2; Sequence=External;
CC -!- DOMAIN: The BAR domain mediates interaction with the exocyst components
CC EXOC4 and EXOC8 and is required for the function in cell migration
CC (PubMed:21658605). It also mediates the interaction with PLXND1
CC (PubMed:24841563). {ECO:0000269|PubMed:21658605,
CC ECO:0000269|PubMed:24841563}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85842.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85842.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR456576; CAG30462.1; -; mRNA.
DR EMBL; AK124370; BAC85842.1; ALT_SEQ; mRNA.
DR EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008282; AAH08282.1; ALT_INIT; mRNA.
DR EMBL; AL157480; CAB75671.2; -; mRNA.
DR CCDS; CCDS13952.2; -. [Q9Y3L3-1]
DR PIR; T46916; T46916.
DR RefSeq; NP_061830.3; NM_018957.3. [Q9Y3L3-1]
DR PDB; 4J9D; X-ray; 1.50 A; B/D/F=616-625.
DR PDB; 4J9F; X-ray; 1.09 A; B/D/F=616-625.
DR PDBsum; 4J9D; -.
DR PDBsum; 4J9F; -.
DR AlphaFoldDB; Q9Y3L3; -.
DR SMR; Q9Y3L3; -.
DR BioGRID; 117149; 41.
DR IntAct; Q9Y3L3; 20.
DR MINT; Q9Y3L3; -.
DR STRING; 9606.ENSP00000350018; -.
DR GlyGen; Q9Y3L3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3L3; -.
DR PhosphoSitePlus; Q9Y3L3; -.
DR BioMuta; SH3BP1; -.
DR DMDM; 51338841; -.
DR CPTAC; CPTAC-1004; -.
DR EPD; Q9Y3L3; -.
DR jPOST; Q9Y3L3; -.
DR MassIVE; Q9Y3L3; -.
DR MaxQB; Q9Y3L3; -.
DR PaxDb; Q9Y3L3; -.
DR PeptideAtlas; Q9Y3L3; -.
DR PRIDE; Q9Y3L3; -.
DR ProteomicsDB; 86041; -. [Q9Y3L3-1]
DR ProteomicsDB; 86042; -. [Q9Y3L3-2]
DR Antibodypedia; 214; 242 antibodies from 33 providers.
DR DNASU; 23616; -.
DR Ensembl; ENST00000417536.5; ENSP00000411979.1; ENSG00000100092.24. [Q9Y3L3-2]
DR Ensembl; ENST00000649765.2; ENSP00000497104.1; ENSG00000100092.24. [Q9Y3L3-1]
DR GeneID; 23616; -.
DR KEGG; hsa:23616; -.
DR MANE-Select; ENST00000649765.2; ENSP00000497104.1; NM_018957.6; NP_061830.3.
DR UCSC; uc003atg.2; human. [Q9Y3L3-1]
DR CTD; 23616; -.
DR DisGeNET; 23616; -.
DR GeneCards; SH3BP1; -.
DR HGNC; HGNC:10824; SH3BP1.
DR HPA; ENSG00000100092; Tissue enhanced (esophagus).
DR MIM; 617368; gene.
DR neXtProt; NX_Q9Y3L3; -.
DR OpenTargets; ENSG00000100092; -.
DR PharmGKB; PA35732; -.
DR VEuPathDB; HostDB:ENSG00000100092; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000158369; -.
DR HOGENOM; CLU_013806_2_0_1; -.
DR InParanoid; Q9Y3L3; -.
DR OMA; IESPRYG; -.
DR OrthoDB; 821331at2759; -.
DR PhylomeDB; Q9Y3L3; -.
DR TreeFam; TF316514; -.
DR PathwayCommons; Q9Y3L3; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q9Y3L3; -.
DR SIGNOR; Q9Y3L3; -.
DR BioGRID-ORCS; 23616; 22 hits in 1075 CRISPR screens.
DR ChiTaRS; SH3BP1; human.
DR GeneWiki; SH3BP1; -.
DR GenomeRNAi; 23616; -.
DR Pharos; Q9Y3L3; Tbio.
DR PRO; PR:Q9Y3L3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9Y3L3; protein.
DR Bgee; ENSG00000100092; Expressed in granulocyte and 100 other tissues.
DR ExpressionAtlas; Q9Y3L3; baseline and differential.
DR Genevisible; Q9Y3L3; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0030215; F:semaphorin receptor binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; IMP:UniProtKB.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Cell junction;
KW Cell projection; Cytoplasm; GTPase activation; Nucleus; Phagocytosis;
KW Phosphoprotein; Reference proteome; SH3-binding; Tight junction.
FT CHAIN 1..701
FT /note="SH3 domain-binding protein 1"
FT /id="PRO_0000056723"
FT DOMAIN 17..262
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 276..469
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..275
FT /note="Interaction with CGNL1"
FT /evidence="ECO:0000269|PubMed:22891260"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..701
FT /note="Interaction with CD2AP"
FT /evidence="ECO:0000269|PubMed:22891260"
FT REGION 496..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 616..625
FT /note="SH3-binding"
FT /evidence="ECO:0000250|UniProtKB:P55194"
FT COMPBIAS 506..522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..632
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZFJ3"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 601
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55194"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55194"
FT VAR_SEQ 440..452
FT /note="DQAQLDAASVSSI -> TEPARELGSQTLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011373"
FT VAR_SEQ 453..701
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011374"
FT VARIANT 511
FT /note="P -> L (in dbSNP:rs929038)"
FT /id="VAR_033450"
FT VARIANT 656
FT /note="S -> F (in dbSNP:rs2269548)"
FT /id="VAR_033451"
FT MUTAGEN 312
FT /note="R->A: Probable loss of the GTPase activator
FT activity. Loss of function in cell migration."
FT /evidence="ECO:0000269|PubMed:21658605"
SQ SEQUENCE 701 AA; 75713 MW; 877D144E81F0F974 CRC64;
MMKRQLHRMR QLAQTGSLGR TPETAEFLGE DLLQVEQRLE PAKRAAHNIH KRLQACLQGQ
SGADMDKRVK KLPLMALSTT MAESFKELDP DSSMGKALEM SCAIQNQLAR ILAEFEMTLE
RDVLQPLSRL SEEELPAILK HKKSLQKLVS DWNTLKSRLS QATKNSGSSQ GLGGSPGSHS
HTTMANKVET LKEEEEELKR KVEQCRDEYL ADLYHFVTKE DSYANYFIRL LEIQADYHRR
SLSSLDTALA ELRENHGQAD HSPSMTATHF PRVYGVSLAT HLQELGREIA LPIEACVMML
LSEGMKEEGL FRLAAGASVL KRLKQTMASD PHSLEEFCSD PHAVAGALKS YLRELPEPLM
TFDLYDDWMR AASLKEPGAR LQALQEVCSR LPPENLSNLR YLMKFLARLA EEQEVNKMTP
SNIAIVLGPN LLWPPEKEGD QAQLDAASVS SIQVVGVVEA LIQSADTLFP GDINFNVSGL
FSAVTLQDTV SDRLASEELP STAVPTPATT PAPAPAPAPA PAPALASAAT KERTESEVPP
RPASPKVTRS PPETAAPVED MARRTKRPAP ARPTMPPPQV SGSRSSPPAP PLPPGSGSPG
TPQALPRRLV GSSLRAPTVP PPLPPTPPQP ARRQSRRSPA SPSPASPGPA SPSPVSLSNP
AQVDLGAATA EGGAPEAISG VPTPPAIPPQ PRPRSLASET N
